甲醛交联与结构蛋白质组学：弥合差距
Formaldehyde cross-linking and structural proteomics: Bridging the gap.
作者信息
Srinivasa Savita, Ding Xuan, Kast Juergen
机构信息
The Biomedical Research Centre, University of British Columbia, Vancouver, BC V6T 1Z3, Canada; Department of Chemistry, University of British Columbia, Vancouver, BC V6T 1Z3, Canada.
The Biomedical Research Centre, University of British Columbia, Vancouver, BC V6T 1Z3, Canada; Department of Chemistry, University of British Columbia, Vancouver, BC V6T 1Z3, Canada; Institute for Genomics, Biocomputing and Biotechnology, Mississippi State University, Mississippi State, MS 39762, United States.
出版信息
Methods. 2015 Nov 1;89:91-8. doi: 10.1016/j.ymeth.2015.05.006. Epub 2015 May 13.
Proteins are dynamic entities constantly moving and altering their structures based on their functions and interactions inside and outside the cell. Formaldehyde cross-linking combined with mass spectrometry can accurately capture interactions of these rapidly changing biomolecules while maintaining their physiological surroundings. Even with its numerous established uses in biology and compatibility with mass spectrometry, formaldehyde has not yet been applied in structural proteomics. However, formaldehyde cross-linking is moving toward analyzing tertiary structure, which conventional cross-linkers have already accomplished. The purpose of this review is to describe the potential of formaldehyde cross-linking in structural proteomics by highlighting its applications, characteristics and current status in the field.
蛋白质是动态实体，它们不断移动并根据其在细胞内外的功能和相互作用改变其结构。甲醛交联结合质谱法可以在维持其生理环境的同时准确捕获这些快速变化的生物分子的相互作用。尽管甲醛在生物学中有众多既定用途且与质谱法兼容，但它尚未应用于结构蛋白质组学。然而，甲醛交联正朝着分析三级结构发展，而传统交联剂已经实现了这一点。本综述的目的是通过强调甲醛交联在该领域的应用、特点和现状，来描述其在结构蛋白质组学中的潜力。
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